|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
422-932 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 800.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 422 LPPLNLLEFDDSQRSAFDRASMLELSARLAQTLENYGVKGEVVAIRPGPVVTMYEFAPAPGTRVNKIANLSDDLAMSLEA 501
Cdd:COG1674 137 LPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 502 LSVRIVAPIPGKAAVGIEVPNKSRETVYLKEVLCDDVFKSGKHKLPLAVGKDIEGAPSVVDLAKMPHLLVAGTTGSGKSV 581
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 582 AVNSMITSLLYSRTPAEVRVIMVDPKMLELSIYEGIPHLLLPVVTDPKKANLALRWGVEEMERRYDLLASMGVRDLGGYN 661
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 662 KKAAKLRAEYEAEKlrraaeaaeraaaaaaanqggdaefddaseeelpplpePPEDLPYIVIIIDEFADLMMCAPKEVET 741
Cdd:COG1674 377 EKVREAKAKGEEEE--------------------------------------GLEPLPYIVVIIDELADLMMVAGKEVEE 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 742 SVARIAQKARAAGIHLVLATQRPSVDVITGLIKANFPSRAAFRVTSKVDSRTILDQGGAEALLGAGDMLFSDRGAS-PCR 820
Cdd:COG1674 419 AIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASkPIR 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 821 YHGCFVDEEEIARVVDFLKQQGQPVYNMDILKPREEEddgnsGGSGGDEVVDEMYDRAVALVSETQQASISMIQRRLRVG 900
Cdd:COG1674 499 VQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEE-----DEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIG 573
|
490 500 510
....*....|....*....|....*....|..
gi 262083198 901 YNRAARMVEQMEREGVVSSPDHTNKREVLIQP 932
Cdd:COG1674 574 YNRAARLIDQMEERGIVGPAEGSKPREVLVSP 605
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
384-932 |
1.41e-179 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 556.62 E-value: 1.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 384 PVIVESRFAKKKPQSDDSGDEANAAKL-----DFIPLHNGTYSLPPLNLLEFDDSQRSAFDRASmLELSARLAQT-LENY 457
Cdd:PRK10263 823 PVAPQPQYQQPQQPVAPQPQDTLLHPLlmrngDSRPLHKPTTPLPSLDLLTPPPSEVEPVDTFA-LEQMARLVEArLADF 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 458 GVKGEVVAIRPGPVVTMYEFAPAPGTRVNKIANLSDDLAMSLEALSVRIVAPIPGKAAVGIEVPNKSRETVYLKEVLCDD 537
Cdd:PRK10263 902 RIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 538 VFKSGKHKLPLAVGKDIEGAPSVVDLAKMPHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPKMLELSIYEGI 617
Cdd:PRK10263 982 KFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGI 1061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 618 PHLLLPVVTDPKKANLALRWGVEEMERRYDLLASMGVRDLGGYNKKAAklraeyEAEKLRRAAEAAERaaaaaaanQGGD 697
Cdd:PRK10263 1062 PHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIA------EADRMMRPIPDPYW--------KPGD 1127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 698 AefddaseeeLPPLPEPPEDLPYIVIIIDEFADLMMCAPKEVETSVARIAQKARAAGIHLVLATQRPSVDVITGLIKANF 777
Cdd:PRK10263 1128 S---------MDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANI 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 778 PSRAAFRVTSKVDSRTILDQGGAEALLGAGDMLFSD-RGASPCRYHGCFVDEEEIARVVDFLKQQGQPVYNMDILKPREE 856
Cdd:PRK10263 1199 PTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGpNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGITSDSES 1278
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262083198 857 EddGNSGGSGGDEVVDEMYDRAVALVSETQQASISMIQRRLRVGYNRAARMVEQMEREGVVSSPDHTNKREVLIQP 932
Cdd:PRK10263 1279 E--GGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
530-765 |
8.71e-62 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 208.77 E-value: 8.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 530 LKEVLCDDVFKSGKHKLPLAVGKDIEGAPSVVDLAKMP-HLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPKM 608
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 609 LELSIYEGIPHLL-LPVVTDPKKANLALRWGVEEMERRYDLLASMGVRDLGGYNKKAAklraeyEAEKLRRAAEAAERAA 687
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIA------EDPLDGFGDVFLVIYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 688 AAAAANQGGDAEfddaseeelpplpeppeDLPYIVIIIDEFADLMMCAPKE----VETSVARIAQKARAAGIHLVLATQR 763
Cdd:pfam01580 155 VHVMCTAGRWLE-----------------ILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQR 217
|
..
gi 262083198 764 PS 765
Cdd:pfam01580 218 PS 219
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
872-931 |
5.11e-29 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 110.20 E-value: 5.11e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 872 DEMYDRAVALVSETQQASISMIQRRLRVGYNRAARMVEQMEREGVVSSPDHTNKREVLIQ 931
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
567-795 |
4.30e-18 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 90.05 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 567 PHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPK---MLELsiYEGIPHLLlPVVT--DPKKANLALRWGVEE 641
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLL-GTITnlDGAQSMRALASIKAE 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 642 MERRYDLLASMGVRDLGGYNKKaaklraeYEAEKlrraaeaaeraaaaaaanqggdaefddaseeelpplpePPEDLPYI 721
Cdd:TIGR03928 547 LKKRQRLFGENNVNHINQYQKL-------YKQGK--------------------------------------AKEPMPHL 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262083198 722 VIIIDEFADLMMCAP---KEVeTSVARIAqkaRAAGIHLVLATQRPSvDVITGLIKANFPSRAAFRVTSKVDSRTIL 795
Cdd:TIGR03928 582 FLISDEFAELKSEQPefmKEL-VSTARIG---RSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
49-189 |
3.17e-10 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 59.91 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 49 REIVGIISLGVAIFLVAALLS-----------LQLGGGT--LMGPFGRTIALGVYGLAGICSYGLVAMLVVGAIRLLREQ 115
Cdd:pfam13491 5 RELLGLALLLLGLFLLLALVSyspadpswstsGSGAAPVhnWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRR 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262083198 116 TPIVRPSEILGGWLGVVSLGAL--LHLAAGDYLVAGHApGGIIGEHVAEIFRAMISTAGTVLLALTGLLSAAIIAT 189
Cdd:pfam13491 85 SLERRWLRLLGFLLLLLASSALfaLRLPSLEFGLPGGA-GGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVT 159
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
568-607 |
4.20e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 38.74 E-value: 4.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 262083198 568 HLLVAGTTGSGKSVAVNSMITsLLYSRTPaevRVIMVDPK 607
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLL-DQAARGG---SVIITDPK 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FtsK |
COG1674 |
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, ... |
422-932 |
0e+00 |
|
DNA segregation ATPase FtsK/SpoIIIE or related protein [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441280 [Multi-domain] Cd Length: 611 Bit Score: 800.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 422 LPPLNLLEFDDSQRSAFDRASMLELSARLAQTLENYGVKGEVVAIRPGPVVTMYEFAPAPGTRVNKIANLSDDLAMSLEA 501
Cdd:COG1674 137 LPPLDLLDPPPPKKEKIDEEELEENARLLEETLEDFGVEAKVVGVTPGPVVTRYEIEPAPGVKVSKITNLADDIALALAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 502 LSVRIVAPIPGKAAVGIEVPNKSRETVYLKEVLCDDVFKSGKHKLPLAVGKDIEGAPSVVDLAKMPHLLVAGTTGSGKSV 581
Cdd:COG1674 217 KSVRIEAPIPGKSAVGIEVPNKKRETVYLREVLESDEFQNSKSPLPIALGKDISGEPVVADLAKMPHLLIAGATGSGKSV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 582 AVNSMITSLLYSRTPAEVRVIMVDPKMLELSIYEGIPHLLLPVVTDPKKANLALRWGVEEMERRYDLLASMGVRDLGGYN 661
Cdd:COG1674 297 CINAMILSLLYKATPDEVRLILIDPKMVELSVYNGIPHLLTPVVTDPKKAANALKWAVREMERRYKLFAKAGVRNIAGYN 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 662 KKAAKLRAEYEAEKlrraaeaaeraaaaaaanqggdaefddaseeelpplpePPEDLPYIVIIIDEFADLMMCAPKEVET 741
Cdd:COG1674 377 EKVREAKAKGEEEE--------------------------------------GLEPLPYIVVIIDELADLMMVAGKEVEE 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 742 SVARIAQKARAAGIHLVLATQRPSVDVITGLIKANFPSRAAFRVTSKVDSRTILDQGGAEALLGAGDMLFSDRGAS-PCR 820
Cdd:COG1674 419 AIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPSRIAFAVSSKIDSRTILDQGGAEKLLGRGDMLFLPPGASkPIR 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 821 YHGCFVDEEEIARVVDFLKQQGQPVYNMDILKPREEEddgnsGGSGGDEVVDEMYDRAVALVSETQQASISMIQRRLRVG 900
Cdd:COG1674 499 VQGAFVSDEEVERVVDFLKSQGEPEYIEEILEEEEEE-----DEGGDDDEDDELFDEAVELVVETQKASTSLLQRRLRIG 573
|
490 500 510
....*....|....*....|....*....|..
gi 262083198 901 YNRAARMVEQMEREGVVSSPDHTNKREVLIQP 932
Cdd:COG1674 574 YNRAARLIDQMEERGIVGPAEGSKPREVLVSP 605
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
384-932 |
1.41e-179 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 556.62 E-value: 1.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 384 PVIVESRFAKKKPQSDDSGDEANAAKL-----DFIPLHNGTYSLPPLNLLEFDDSQRSAFDRASmLELSARLAQT-LENY 457
Cdd:PRK10263 823 PVAPQPQYQQPQQPVAPQPQDTLLHPLlmrngDSRPLHKPTTPLPSLDLLTPPPSEVEPVDTFA-LEQMARLVEArLADF 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 458 GVKGEVVAIRPGPVVTMYEFAPAPGTRVNKIANLSDDLAMSLEALSVRIVAPIPGKAAVGIEVPNKSRETVYLKEVLCDD 537
Cdd:PRK10263 902 RIKADVVNYSPGPVITRFELNLAPGVKAARISNLSRDLARSLSTVAVRVVEVIPGKPYVGLELPNKKRQTVYLREVLDNA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 538 VFKSGKHKLPLAVGKDIEGAPSVVDLAKMPHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPKMLELSIYEGI 617
Cdd:PRK10263 982 KFRDNPSPLTVVLGKDIAGEPVVADLAKMPHLLVAGTTGSGKSVGVNAMILSMLYKAQPEDVRFIMIDPKMLELSVYEGI 1061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 618 PHLLLPVVTDPKKANLALRWGVEEMERRYDLLASMGVRDLGGYNKKAAklraeyEAEKLRRAAEAAERaaaaaaanQGGD 697
Cdd:PRK10263 1062 PHLLTEVVTDMKDAANALRWCVNEMERRYKLMSALGVRNLAGYNEKIA------EADRMMRPIPDPYW--------KPGD 1127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 698 AefddaseeeLPPLPEPPEDLPYIVIIIDEFADLMMCAPKEVETSVARIAQKARAAGIHLVLATQRPSVDVITGLIKANF 777
Cdd:PRK10263 1128 S---------MDAQHPVLKKEPYIVVLVDEFADLMMTVGKKVEELIARLAQKARAAGIHLVLATQRPSVDVITGLIKANI 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 778 PSRAAFRVTSKVDSRTILDQGGAEALLGAGDMLFSD-RGASPCRYHGCFVDEEEIARVVDFLKQQGQPVYNMDILKPREE 856
Cdd:PRK10263 1199 PTRIAFTVSSKIDSRTILDQAGAESLLGMGDMLYSGpNSTLPVRVHGAFVRDQEVHAVVQDWKARGRPQYVDGITSDSES 1278
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262083198 857 EddGNSGGSGGDEVVDEMYDRAVALVSETQQASISMIQRRLRVGYNRAARMVEQMEREGVVSSPDHTNKREVLIQP 932
Cdd:PRK10263 1279 E--GGAGGFDGAEELDPLFDQAVQFVTEKRKASISGVQRQFRIGYNRAARIIEQMEAQGIVSEQGHNGNREVLAPP 1352
|
|
| FtsK_SpoIIIE |
pfam01580 |
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from ... |
530-765 |
8.71e-62 |
|
FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.
Pssm-ID: 279863 [Multi-domain] Cd Length: 219 Bit Score: 208.77 E-value: 8.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 530 LKEVLCDDVFKSGKHKLPLAVGKDIEGAPSVVDLAKMP-HLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPKM 608
Cdd:pfam01580 1 LLEVLESKPFDTDYSRLPIALGKDISGNPEVFDLKKMPvHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 609 LELSIYEGIPHLL-LPVVTDPKKANLALRWGVEEMERRYDLLASMGVRDLGGYNKKAAklraeyEAEKLRRAAEAAERAA 687
Cdd:pfam01580 81 GELSAYEDIPHLLsVPVATDPKRALRALEWLVDEMERRYALFRALGVRSIAGYNGEIA------EDPLDGFGDVFLVIYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 688 AAAAANQGGDAEfddaseeelpplpeppeDLPYIVIIIDEFADLMMCAPKE----VETSVARIAQKARAAGIHLVLATQR 763
Cdd:pfam01580 155 VHVMCTAGRWLE-----------------ILPYLVVIVDERAELRLAAPKDsemrVEDAIVRLAQKGRAAGIHLLLATQR 217
|
..
gi 262083198 764 PS 765
Cdd:pfam01580 218 PS 219
|
|
| FtsK_alpha |
pfam17854 |
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell ... |
422-522 |
1.64e-42 |
|
FtsK alpha domain; FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. FtsK can be split into three domains called alpha (this entry), beta and gamma. The alpha and beta domains contain the core ATPase machinery of the DNA translocase.
Pssm-ID: 436096 [Multi-domain] Cd Length: 101 Bit Score: 149.99 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 422 LPPLNLLEFDDSQRSAFDRASMLELSARLAQTLENYGVKGEVVAIRPGPVVTMYEFAPAPGTRVNKIANLSDDLAMSLEA 501
Cdd:pfam17854 1 LPPLDLLEPPPTSSQKVDEEELEETAEKLEETLAEFGIEAKVVGVTPGPVVTLYELEPAPGVKVSKITNLSDDLALALSA 80
|
90 100
....*....|....*....|.
gi 262083198 502 LSVRIVAPIPGKAAVGIEVPN 522
Cdd:pfam17854 81 PSIRIVAPIPGKSTIGIEVPN 101
|
|
| FtsK_gamma |
pfam09397 |
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix ... |
872-931 |
1.01e-29 |
|
Ftsk gamma domain; This domain directs oriented DNA translocation and forms a winged helix structure. Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 462786 [Multi-domain] Cd Length: 63 Bit Score: 112.08 E-value: 1.01e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 872 DEMYDRAVALVSETQQASISMIQRRLRVGYNRAARMVEQMEREGVVSSPDHTNKREVLIQ 931
Cdd:pfam09397 4 DELYEEAVEIVIETGKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPADGSKPREVLIT 63
|
|
| Ftsk_gamma |
smart00843 |
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated ... |
872-931 |
5.11e-29 |
|
This domain directs oriented DNA translocation and forms a winged helix structure; Mutated proteins with substitutions in the FtsK gamma DNA-recognition helix are impaired in DNA binding.
Pssm-ID: 197911 [Multi-domain] Cd Length: 63 Bit Score: 110.20 E-value: 5.11e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 872 DEMYDRAVALVSETQQASISMIQRRLRVGYNRAARMVEQMEREGVVSSPDHTNKREVLIQ 931
Cdd:smart00843 4 DELYDEAVELVIETQKASTSLLQRRLRIGYNRAARLIDQLEEEGIVGPANGSKPREVLVT 63
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
567-795 |
4.30e-18 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 90.05 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 567 PHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPK---MLELsiYEGIPHLLlPVVT--DPKKANLALRWGVEE 641
Cdd:TIGR03928 470 PHGLVAGTTGSGKSEILQTYILSLAVNFHPHEVAFLLIDYKgggMANL--FKNLPHLL-GTITnlDGAQSMRALASIKAE 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 642 MERRYDLLASMGVRDLGGYNKKaaklraeYEAEKlrraaeaaeraaaaaaanqggdaefddaseeelpplpePPEDLPYI 721
Cdd:TIGR03928 547 LKKRQRLFGENNVNHINQYQKL-------YKQGK--------------------------------------AKEPMPHL 581
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262083198 722 VIIIDEFADLMMCAP---KEVeTSVARIAqkaRAAGIHLVLATQRPSvDVITGLIKANFPSRAAFRVTSKVDSRTIL 795
Cdd:TIGR03928 582 FLISDEFAELKSEQPefmKEL-VSTARIG---RSLGVHLILATQKPS-GVVDDQIWSNSRFKLALKVQDASDSNEIL 653
|
|
| T7SS_EccC_a |
TIGR03924 |
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit ... |
547-800 |
2.27e-10 |
|
type VII secretion protein EccCa; This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274858 [Multi-domain] Cd Length: 658 Bit Score: 64.61 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 547 PLAVGKDieGAPSVVDLAK-----M-PHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPK----MLELsiyEG 616
Cdd:TIGR03924 412 PIGVGDD--GEPVELDLKEsaeggMgPHGLCIGATGSGKSELLRTLVLGLAATHSPEQLNLVLVDFKggatFLGL---EG 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 617 IPHLLlPVVTD-PKKANLALR-----WGveEMERRYDLLASMG-VRDLGGYNKkaakLRAeyeaeklrraaeaaeraaaa 689
Cdd:TIGR03924 487 LPHVS-AVITNlADEAPLVDRmqdalAG--EMNRRQELLRAAGnFANVAEYEK----ARA-------------------- 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 690 aaanQGGDAEfddaseeelpplpeppeDLPYIVIIIDEFADLMMCAPKEVETSVArIAQKARAAGIHLVLATQRPSVDVI 769
Cdd:TIGR03924 540 ----AGADLP-----------------PLPALFVVVDEFSELLSQHPDFADLFVA-IGRLGRSLGVHLLLASQRLDEGRL 597
|
250 260 270
....*....|....*....|....*....|.
gi 262083198 770 TGLiKANFPSRAAFRVTSKVDSRTILDQGGA 800
Cdd:TIGR03924 598 RGL-ESHLSYRIGLKTFSASESRAVLGVPDA 627
|
|
| FtsK_4TM |
pfam13491 |
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the ... |
49-189 |
3.17e-10 |
|
4TM region of DNA translocase FtsK/SpoIIIE; 4TM_FtsK is the integral membrane domain of the FtsK DNA tranlocases. During sporulation in Bacillus subtilis, the SpoIIIE protein is believed to form a translocation pore at the leading edge of the nearly closed septum. The E. coli FtsK protein is homologous to SpoIIIE, and can free chromosomes trapped in vegetative septa.
Pssm-ID: 463896 Cd Length: 171 Bit Score: 59.91 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 49 REIVGIISLGVAIFLVAALLS-----------LQLGGGT--LMGPFGRTIALGVYGLAGICSYGLVAMLVVGAIRLLREQ 115
Cdd:pfam13491 5 RELLGLALLLLGLFLLLALVSyspadpswstsGSGAAPVhnWGGRFGAWLADLLLQLFGYSAWLLPVALLYWGWRLFRRR 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262083198 116 TPIVRPSEILGGWLGVVSLGAL--LHLAAGDYLVAGHApGGIIGEHVAEIFRAMISTAGTVLLALTGLLSAAIIAT 189
Cdd:pfam13491 85 SLERRWLRLLGFLLLLLASSALfaLRLPSLEFGLPGGA-GGVIGRLLANALVTLLGFTGATLLLLALLAIGLSLVT 159
|
|
| T7_EssCb_Firm |
TIGR03928 |
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, ... |
558-795 |
3.31e-06 |
|
type VII secretion protein EssC, C-terminal domain; This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274860 [Multi-domain] Cd Length: 1296 Bit Score: 51.14 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 558 PSVVDLAKMPHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPKMLELSIYEGIPHlLLPVVT--DPKKANLAL 635
Cdd:TIGR03928 802 PLTLDLSKDGHLAIFGSPGYGKSTFLQTLIMSLARQHSPEQLHFYLFDFGTNGLLPLKKLPH-VADYFTldEEEKIEKLI 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 636 RWGVEEMERRYDLLASMGVRDLGGYNKKAaklraeyeAEKLRRaaeaaeraaaaaaanqggdaefddaseeelpplpepp 715
Cdd:TIGR03928 881 RRIKKEIDRRKKLFSEYGVASISMYNKAS--------GEKLPQ------------------------------------- 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 716 edlpyIVIIIDEFaDLMMCAP--KEVETSVARIAQKARAAGIHLVL-ATQRPSVDVItglIKANFPSRAAFRVTSKVDSR 792
Cdd:TIGR03928 916 -----IVIIIDNY-DAVKEEPfyEDFEELLIQLAREGASLGIYLVMtAGRQNAVRMP---LMNNIKTKIALYLIDKSEYR 986
|
...
gi 262083198 793 TIL 795
Cdd:TIGR03928 987 SIV 989
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
547-607 |
1.04e-05 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 48.84 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262083198 547 PLAVGKDI-EGAPSVVDLAKM--PHLLVAGTTGSGKSVAVNSMITSLLysrtPAEVRVIMVDPK 607
Cdd:COG0433 25 GILIGKLLsPGVPVYLDLDKLlnRHILILGATGSGKSNTLQVLLEELS----RAGVPVLVFDPH 84
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
567-606 |
2.39e-05 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 48.02 E-value: 2.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 262083198 567 PHLLVAGTTGSGKSVAVNSMITSLLYSRTpaevRVIMVDP 606
Cdd:COG3451 205 GNTLILGPSGSGKSFLLKLLLLQLLRYGA----RIVIFDP 240
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
488-607 |
4.13e-05 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 47.29 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262083198 488 IANLSDDLAMSLEALSVRIVAPIPGKAAVGIEV-PnksrETVYLKEVLCDDVFksGKHKLPLAVGkDIEGAPSVVDLAKM 566
Cdd:TIGR03925 291 LDGIASVDDLGTRGLVAVIRDVWGGPPAPPVRLlP----ARLPLSALPAGGGA--PRLRVPLGLG-ESDLAPVYVDFAES 363
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 262083198 567 PHLLVAGTTGSGKSVAVNSMITSLLYSRTPAEVRVIMVDPK 607
Cdd:TIGR03925 364 PHLLIFGDSESGKTTLLRTIARGIVRRYSPDQARLVVVDYR 404
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
568-607 |
4.20e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 38.74 E-value: 4.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 262083198 568 HLLVAGTTGSGKSVAVNSMITsLLYSRTPaevRVIMVDPK 607
Cdd:cd01127 1 NTLVLGTTGSGKTTSIVIPLL-DQAARGG---SVIITDPK 36
|
|
| |
